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69022 Thrombin Cleavage Capture Kit

69022
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      Description
      OverviewThe Thrombin Cleavage Capture Kit is designed for cleavage of fusion proteins followed by convenient and quantitative removal of thrombin protease. The method is based on the use of Biotinylated Thrombin for digestion and its subsequent removal with Streptavidin Agarose. The kit is suitable for use with any fusion protein that contains a thrombin recognition sequence. A Cleavage Control Protein is included in the kit to monitor performance of cleavage conditions. It is cleaved into 2 fragments, which are easily visualized by SDS-PAGE.

      The Cleavage Control Protein is also available separately to monitor performance of either thrombin or enterokinase cleavage conditions. The 48 kDa control protein is cleaved into two proteolytic fragments of 35 kDa and 13 kDa, which are easily visualized by SDS-PAGE.

      Catalogue Number69022
      Brand Family Novagen®
      References
      Product Information
      Components
      Applications
      Biological Information
      Physicochemical Information
      Dimensions
      Materials Information
      Toxicological Information
      Safety Information according to GHS
      Safety Information
      R PhraseR: 36/37/38

      Irritating to eyes, respiratory system and skin.
      S PhraseS: 26-36

      In case of contact with eyes, rinse immediately with plenty of water and seek medical advice.
      Wear suitable protective clothing.
      Product Usage Statements
      Storage and Shipping Information
      Ship Code Blue Ice Only
      Toxicity Multiple Toxicity Values, refer to MSDS
      Storage Multiple storage requirements
      Avoid freeze/thaw Avoid freeze/thaw
      Do not freeze Ok to freeze
      Packaging Information
      Transport Information
      Supplemental Information
      Specifications

      Documentation

      Thrombin Cleavage Capture Kit Certificates of Analysis

      TitleLot Number
      69022

      Citations

      Title
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    • Amélie Fradet-Turcotte, et al. (2007) Quantitative analysis of the binding of simian virus 40 large T antigen to DNA. Journal of Virology 81, 9162-9174.
    • Galina D. Kutuzova, et al. (2006) Calbindin D9k knockout mice are indistinguishable from wild-type mice in phenotype and serum calcium level. Procedings of the National Academy of Science 103, 12377-12381.
    • David Shaya, et al. (2006) Crystal structure of heparinase II from Pedobacter heparinus and its complex with a disaccharide product. Journal of Biological Chemistry 281, 15525-15535.
    • Juan Luis Asensio, et al. (2005) Structure of the functional domain of 29 replication organizer: insights into oligomerization and DNA binding. Journal of Biological Chemistry 280, 20730-20739.
    • Marcelo Comini, et al. (2005) Trypanothione synthesis in Crithidia revisited. Journal of Biological Chemistry 280, 6850-6860.
    • Yong Hoon Lee, et al. (2005) Use of dominant-negative HrpA mutants to dissect Hrp pilus assembly and type III secretion in Pseudomonas syringae pv. tomato. Journal of Biological Chemistry 280, 21409-21417.
    • Roberta Leonardi, et al. (2005) A pantothenate kinase from Staphylococcus aureus refractory to feedback regulation by coenzyme A. Journal of Biological Chemistry 280, 3314-3322.
    • Subhradip Mukhopadhyay, et al. (2005) Identification of a region of fast skeletal troponin T required for stabilization of the coiled-coil formation with troponin I. Journal of Biological Chemistry 280, 538-547.
    • Angela K. Nevins and Debbie C. Thurmond. (2005) A direct interaction between Cdc42 and vesicle-associated membrane protein 2 regulates SNARE-dependent insulin exocytosis. Journal of Biological Chemistry 280, 1944-1952.
    • Angela W. Norton, et al. (2005) Evaluation of the 17-kDa prenyl-binding protein as a regulatory protein for phototransduction in retinal photoreceptors. Journal of Biological Chemistry 280, 1248-1256.
    • Natasha Pashkova, et al. (2005) Myosin V attachment to cargo requires the tight association of two functional subdomains. Journal of Cell Biology 168, 359-364.
    • J. Jefferson Smith, et al. (2005) Orthogonal site-specific protein modification by engineering reversible thiol protection mechanisms. Protein Science 14, 64-73.
    • Katalin Fejes Tóth, Jacek Mazurkiewicz and Karsten Rippe. (2005) Association states of nucleosome assembly protein 1 and its complexes with histones. Journal of Biological Chemistry 280, 15690-15699.
    • Esther Wong, et al. (2005) Expression and characterization of soluble amino-terminal domain of NR2B subunit of N-methyl-D-aspartate receptor. Protein Science 14, 2275-2283.
    • Liangwen Xiong, et al. (2005) Sites on calmodulin that interact with the C-terminal tail of Cav1.2 channel. Journal of Biological Chemistry 280, 7070-7079.
    • David M. Rancour, et al. (2004) Plant UBX domain-containing protein 1, PUX1, regulates the oligomeric structure and activity of Arabidopsis CDC48. Journal of Biological Chemistry 279, 54264-54274.
    • Kunhong Xiao, et al. (2004) Activation-dependent conformational changes in β-arrestin 2. Journal of Biological Chemistry 279, 55744-55753.
    • T.L. Grimek, et al. (2003) Residues C123 and D58 of the 2-methlisocitrate lyase (PrpB) enzyme of Salmonella enterica are essential for catalysis. Journal of Bacteriology 185, 4837-4843.
    • H.Q. Xu, et al. (2003) Simultaneously monitoring DNA binding and helicase-catalyzed DNA unwinding by fluorescence polarization. Nucleic Acids Research 31,.
    • User Protocols

      Title
      TB188 Thrombin Kits